EaStCHEM School of Chemistry, Biomedical Sciences Research Complex, and Centre of Magnetic Resonance, University of St Andrews, St Andrews, KY16 9ST, UK.
School of Medicine, Biomedical Sciences Research Complex, and Centre of Magnetic Resonance, University of St Andrews, St Andrews, KY16 9TF, UK.
Dalton Trans. 2024 Aug 13;53(32):13529-13536. doi: 10.1039/d4dt00892h.
Human serum albumin (HSA) is the most abundant plasma protein, which functions to transport a large range of ligands within the circulation. These interactions have important implications for human health and disease. The primary binding site for Cu ions on HSA is known to be the so-called amino-terminal Cu and Ni binding (ATCUN) motif. However, the number and identity of secondary binding sites is currently not understood. In this study, we harnessed a suite of contemporary electron paramagnetic resonance (EPR) spectroscopy methods to investigate recombinantly produced constructs of HSA bearing single-histidine knockouts, with the aim to characterise its endogenous Cu ion binding sites.
人血清白蛋白（HSA）是最丰富的血浆蛋白，其功能是在循环系统中运输大量配体。这些相互作用对人类健康和疾病有重要意义。已知 HSA 上 Cu 离子的主要结合位点是所谓的氨基末端 Cu 和 Ni 结合（ATCUN）基序。然而，目前尚不清楚次要结合位点的数量和身份。在这项研究中，我们利用一系列现代电子顺磁共振（EPR）光谱方法来研究携带单个组氨酸敲除的重组 HSA 构建体，旨在表征其内源性 Cu 离子结合位点。
